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Investigations into small molecule non-peptidic inhibitors of the botulinum neurotoxins

Academic Article
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Overview

authors

  • Capkova, K.
  • Salzameda, N. T.
  • Janda, Kim

publication date

  • October 2009

journal

  • Toxicon  Journal

abstract

  • Botulinum neurotoxins (BoNTs), proteins secreted by the bacteria genus Clostridium, represent a group of extremely lethal toxins and a potential bioterrorism threat. As the current therapeutic options are of a predominantly prophylactic nature and cannot be used en masse, new strategies and ultimately potential treatments are desperately needed to combat any widespread release of these neurotoxins. In these regards, our laboratory has been working on developing new alternatives to treat botulinum intoxication through the development of inhibitors of the light chain proteases, the etiological agent which causes BoNT intoxication. Such a strategy has required the construction of two high-throughput screens and small molecule non-peptidic libraries; excitingly, inhibitors of the BoNT/A protease have been uncovered and are being optimized via structure activity relationship studies.

subject areas

  • Animals
  • Botulinum Antitoxin
  • Botulinum Toxins
  • Combinatorial Chemistry Techniques
  • Drug Design
  • Humans
  • Neurotoxins
  • Protease Inhibitors
  • Protein Subunits
  • Structure-Activity Relationship
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Research

keywords

  • Botulinum neurotoxin A
  • Botulinum neurotoxin B
  • Botulism
  • Light chain metalloprotease
  • Protease inhibitors
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Identity

PubMed Central ID

  • PMC2730986

International Standard Serial Number (ISSN)

  • 0041-0101

Digital Object Identifier (DOI)

  • 10.1016/j.toxicon.2009.03.016

PubMed ID

  • 19327377
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Additional Document Info

start page

  • 575

end page

  • 582

volume

  • 54

issue

  • 5

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